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Conserved domains on  [gi|1622895688|ref|XP_014979960|]
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netrin-5 [Macaca mulatta]

Protein Classification

calcium-binding EGF-like domain-containing protein; attractin family protein( domain architecture ID 10043567)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions| attractin family protein similar to middle and C-terminal regions of Homo sapiens attractin that is involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 358-473 1.47e-48

NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called domain C in the context of C. elegans netrin UNC-6. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. These proteins may be chemoattractive to some neurons and chemorepellant for others. In the case of netrin-1, attraction and repulsion responses are mediated by the DCC and UNC-5 receptor families. The biological activities of C. elegans UNC-6, which may either attract or repel migrating cells or axons, are mediated by its different domains. The C-terminal NTR domain of UNC-6 has been shown to inhibit axon branching activity.


:

Pssm-ID: 239634  Cd Length: 115  Bit Score: 162.80  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895688 358 LRRYCQQDYVLRAQVLASEAAGPaWRRLAVRVQAVYKQRAQFVRRGDQDAWVPRADLACGCLRLQPGTDYLLLGSVVGGP 437
Cdd:cd03579     1 LKKYCKKDYAVQAQVLSRETAGE-WAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGKDEDSP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622895688 438 DPTRLILDRHGLALPWRPRWARPLRRLQQEERAGGC 473
Cdd:cd03579    80 ERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 272-321 1.04e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 56.98  E-value: 1.04e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622895688 272 ACQCHPIGATGGTCNQTSGQCTCKLGVTGLTCNRCGPGYQQSRSPRMPCQ 321
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 209-263 2.26e-05

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 41.57  E-value: 2.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622895688 209 PCSCNQHA---RRCRFNSelfrlsggrsgGVCErCRHHTAGRHCHYCQPGFWRDPSQP 263
Cdd:cd00055     1 PCDCNGHGslsGQCDPGT-----------GQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
 
Name Accession Description Interval E-value
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 358-473 1.47e-48

NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called domain C in the context of C. elegans netrin UNC-6. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. These proteins may be chemoattractive to some neurons and chemorepellant for others. In the case of netrin-1, attraction and repulsion responses are mediated by the DCC and UNC-5 receptor families. The biological activities of C. elegans UNC-6, which may either attract or repel migrating cells or axons, are mediated by its different domains. The C-terminal NTR domain of UNC-6 has been shown to inhibit axon branching activity.


Pssm-ID: 239634  Cd Length: 115  Bit Score: 162.80  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895688 358 LRRYCQQDYVLRAQVLASEAAGPaWRRLAVRVQAVYKQRAQFVRRGDQDAWVPRADLACGCLRLQPGTDYLLLGSVVGGP 437
Cdd:cd03579     1 LKKYCKKDYAVQAQVLSRETAGE-WAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGKDEDSP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622895688 438 DPTRLILDRHGLALPWRPRWARPLRRLQQEERAGGC 473
Cdd:cd03579    80 ERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 359-466 5.28e-28

UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (pfam00965). This expanded domain family has been named as the NTR module.


Pssm-ID: 396359  Cd Length: 106  Bit Score: 107.43  E-value: 5.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895688 359 RRYCQQ-DYVLRAQVLASEAAGpAWRRLAVRVQAVYKQRAQFVRRGDQDAWVPRADlaCGCLRLQPGTDYLLLGSVVGGP 437
Cdd:pfam01759   1 KKACKGsDYVYKVKVLSVEEEG-SFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD--CRCPQLRLGKEYLIMGKVGDLE 77

                          90       100
                  ....*....|....*....|....*....
gi 1622895688 438 DPTRLILDRHGLALPWRPRWARPLRRLQQ 466
Cdd:pfam01759  78 GRGRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
365-466 2.80e-16

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 74.71  E-value: 2.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895688  365 DYVLRAQVLASEAAGpAWRRLAVRVQAVYKQRAQFVRRGDQDAWVPRADLACGC-LRLQPGTDYLLLGSVV---GGPDPT 440
Cdd:smart00643  10 DYVYKVKVLSVEEEG-GFDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCpLLLKLGKSYLIMGKSGdlwDAKGRG 88

                           90       100
                   ....*....|....*....|....*.
gi 1622895688  441 RLILDRHGLALPWRPRWARPLRRLQQ 466
Cdd:smart00643  89 QYVLGKNSWVEEWPTEEECRLRRLQK 114
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 272-321 1.04e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 56.98  E-value: 1.04e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622895688 272 ACQCHPIGATGGTCNQTSGQCTCKLGVTGLTCNRCGPGYQQSRSPRMPCQ 321
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
273-310 4.57e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.01  E-value: 4.57e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1622895688  273 CQCHPIGATGGTCNQTSGQCTCKLGVTGLTCNRCGPGY 310
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 273-310 1.30e-09

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 53.51  E-value: 1.30e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622895688 273 CQCHPIGATGGTCNQTSGQCTCKLGVTGLTCNRCGPGY 310
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 209-263 2.26e-05

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 41.57  E-value: 2.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622895688 209 PCSCNQHA---RRCRFNSelfrlsggrsgGVCErCRHHTAGRHCHYCQPGFWRDPSQP 263
Cdd:cd00055     1 PCDCNGHGslsGQCDPGT-----------GQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 232-263 1.28e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 39.64  E-value: 1.28e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622895688 232 RSGGVCeRCRHHTAGRHCHYCQPGFWRDPSQP 263
Cdd:pfam00053  15 PETGQC-LCKPGVTGRHCDRCKPGYYGLPSDP 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
234-260 2.03e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 36.14  E-value: 2.03e-03
                           10        20
                   ....*....|....*....|....*..
gi 1622895688  234 GGVCErCRHHTAGRHCHYCQPGFWRDP 260
Cdd:smart00180  17 TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
 
Name Accession Description Interval E-value
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 358-473 1.47e-48

NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called domain C in the context of C. elegans netrin UNC-6. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. These proteins may be chemoattractive to some neurons and chemorepellant for others. In the case of netrin-1, attraction and repulsion responses are mediated by the DCC and UNC-5 receptor families. The biological activities of C. elegans UNC-6, which may either attract or repel migrating cells or axons, are mediated by its different domains. The C-terminal NTR domain of UNC-6 has been shown to inhibit axon branching activity.


Pssm-ID: 239634  Cd Length: 115  Bit Score: 162.80  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895688 358 LRRYCQQDYVLRAQVLASEAAGPaWRRLAVRVQAVYKQRAQFVRRGDQDAWVPRADLACGCLRLQPGTDYLLLGSVVGGP 437
Cdd:cd03579     1 LKKYCKKDYAVQAQVLSRETAGE-WAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGKDEDSP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622895688 438 DPTRLILDRHGLALPWRPRWARPLRRLQQEERAGGC 473
Cdd:cd03579    80 ERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 359-466 5.28e-28

UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (pfam00965). This expanded domain family has been named as the NTR module.


Pssm-ID: 396359  Cd Length: 106  Bit Score: 107.43  E-value: 5.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895688 359 RRYCQQ-DYVLRAQVLASEAAGpAWRRLAVRVQAVYKQRAQFVRRGDQDAWVPRADlaCGCLRLQPGTDYLLLGSVVGGP 437
Cdd:pfam01759   1 KKACKGsDYVYKVKVLSVEEEG-SFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD--CRCPQLRLGKEYLIMGKVGDLE 77

                          90       100
                  ....*....|....*....|....*....
gi 1622895688 438 DPTRLILDRHGLALPWRPRWARPLRRLQQ 466
Cdd:pfam01759  78 GRGRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
365-466 2.80e-16

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 74.71  E-value: 2.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895688  365 DYVLRAQVLASEAAGpAWRRLAVRVQAVYKQRAQFVRRGDQDAWVPRADLACGC-LRLQPGTDYLLLGSVV---GGPDPT 440
Cdd:smart00643  10 DYVYKVKVLSVEEEG-GFDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCpLLLKLGKSYLIMGKSGdlwDAKGRG 88

                           90       100
                   ....*....|....*....|....*.
gi 1622895688  441 RLILDRHGLALPWRPRWARPLRRLQQ 466
Cdd:smart00643  89 QYVLGKNSWVEEWPTEEECRLRRLQK 114
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 361-464 9.62e-13

NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex.


Pssm-ID: 239600  Cd Length: 105  Bit Score: 64.41  E-value: 9.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895688 361 YCQQDYVLRAQVL-ASEAAGpaWRRLAVRVQAVYKQRAQFVRRGDQDAWVPRADLACGCLRLQPGTDYLLLGSVVGGPDp 439
Cdd:cd03523     3 FCKSDYVVRAKIKeIKEEND--DVKYEVKIIKIYKTGKAKADKADLRFYYTAPACCPCHPILNPGREYLIMGKEEDSQG- 79

                          90       100
                  ....*....|....*....|....*
gi 1622895688 440 tRLILDRHGLALPWRPRWARPLRRL 464
Cdd:cd03523    80 -GLVLDPLSFVEPWSPLSLRQDRRL 103
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 272-321 1.04e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 56.98  E-value: 1.04e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622895688 272 ACQCHPIGATGGTCNQTSGQCTCKLGVTGLTCNRCGPGYQQSRSPRMPCQ 321
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
273-310 4.57e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.01  E-value: 4.57e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1622895688  273 CQCHPIGATGGTCNQTSGQCTCKLGVTGLTCNRCGPGY 310
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 273-310 1.30e-09

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 53.51  E-value: 1.30e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622895688 273 CQCHPIGATGGTCNQTSGQCTCKLGVTGLTCNRCGPGY 310
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 209-263 2.26e-05

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 41.57  E-value: 2.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622895688 209 PCSCNQHA---RRCRFNSelfrlsggrsgGVCErCRHHTAGRHCHYCQPGFWRDPSQP 263
Cdd:cd00055     1 PCDCNGHGslsGQCDPGT-----------GQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 232-263 1.28e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 39.64  E-value: 1.28e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622895688 232 RSGGVCeRCRHHTAGRHCHYCQPGFWRDPSQP 263
Cdd:pfam00053  15 PETGQC-LCKPGVTGRHCDRCKPGYYGLPSDP 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
234-260 2.03e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 36.14  E-value: 2.03e-03
                           10        20
                   ....*....|....*....|....*..
gi 1622895688  234 GGVCErCRHHTAGRHCHYCQPGFWRDP 260
Cdd:smart00180  17 TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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